The LamR is a nonintegrin cell-surface protein that has been identified as the receptor for, among others, the extracellular matrix molecule laminin-1 (Rao 1983), pathogenic prion protein. (Gauczynski 2001), Sindbis virus (Wang 1992), Venezuelan equine encephalitis virus (VEE) (Ludwig 1996), cytotoxic necrotizing factor type I and II (McNichol 2007), and Adeno-associated virus serotypes 2, 3, 8 and 9 (Akache 2006). LamR binds to laminin with high affinity, mediating interactions between laminin and the extracellular environment that affect cell adhesion, tumor growth and metastasis.
Two types of LamR, the 67 kDa and the 37 kDa, are found on the surface of cells (Gauczynski 2001.). The 67 kDa laminin receptor may be formed by the dimerization of the 37 kDa laminin receptor. Phylogenetic analysis also suggests that the LamR is a ribosomal protein that acquired the additional novel function of the laminin receptor during evolution (Ardini 1998).
Structural characterization of the LamR may permit greater understanding of how the LamR interacts with its binding partners. This in turn may facilitate development of therapeutics that may block and/or mimic LamR interactions in the setting of, among others, AD, other neurological disorders, cancer, and viral and bacterial infections.
In addition, structural analysis of the LamR may provide insight into the development of therapeutics that aid in the prevention of various disease states, including tumor growth and metastasis.
Because of the role of LamR interaction, with laminin in normal and cancerous cells, as well as its role as a receptor for Sindbis virus, adeno-associated virus and pathogenic prion protein, it is desirable to study LamR using crystallographic methods.